检索规则说明:AND代表“并且”;OR代表“或者”;NOT代表“不包含”;(注意必须大写,运算符两边需空一格)
检 索 范 例 :范例一: (K=图书馆学 OR K=情报学) AND A=范并思 范例二:J=计算机应用与软件 AND (U=C++ OR U=Basic) NOT M=Visual
作 者:罗舒怀 张莹[1] 吴琼芳[1] 彭倩倩[1] 李爱芬[1] 张成武[1]
机构地区:[1]暨南大学生态学系,广州510632
出 处:《植物生理学报》2015年第9期1425-1432,共8页Plant Physiology Journal
基 金:国家自然科学基金(41176105);中央高校基本科研业务费专项资金(21614101)
摘 要:以产油绿藻尖状栅藻(Scenedesmus acuminatus)为实验材料,采用77 K低温荧光、SDS-PAGE圆盘电泳、i TRAQ蛋白定量等方法,研究其在低氮胁迫产油条件下,藻细胞的低温荧光特性及光合色素蛋白复合物的变化。结果表明,在77 K低温条件下尖状栅藻有3个荧光发射峰,分别位于685、695和715 nm处。利用圆盘电泳从藻细胞类囊体膜上分离到6个条带,从上至下依次为CPIa、CPI、CPa1、CPa2、LHCP和FP(游离色素),与对照组(18 mmol·L-1 Na NO3)相比,低氮(3.6 mmol·L-1Na NO3)培养的藻细胞光能耗散增强,分离的类囊体膜色素蛋白复合物代表PSII的条带CPa1和C Pa2模糊,D1蛋白及捕光色素蛋白表达下调。综上低氮限制条件下产油尖状栅藻的PSII核心复合物降解,制约藻细胞吸收和转化光能,进而影响光合效率。In this study, the photosynthetic apparatus of S. acuminatus was analyzed by purifying the thylakoids and isolating the different pigment-protein complexes upon solubilization. In addition, the effects of N-depleted on photosynthetic apparatus were investigated using SDS-PAGE, 77 K fluorescence and isobaric tags for relative and absolute quantification(i TRAQ). The results showed that, six pigment complexes bands including CPIa, CPI, CPa1, CPa2, LHCP, and FP were isolated from the thylakoid membrane of S. acuminatus. Under N-depleted conditions, the bands CPa1, CPa2 which represented PSII became very vague, meanwhile D1 protein and light-harvesting proteins were down-regulated. The 77 K fluorescence spectra of PSI and PSII were located at 685, 695 and 715 nm. The results from the biochemical and spectroscopic characterization showed that, during the culture period, effects of N-depleted on PSII was greater than PSI, while algal cells decreased light utilization and increased dissipation. So we concluded that, there was difference between microaglal and high plant on photosynthetic traits, otherwise the damage of PSII complexes of S. acuminatus in N-depleted conditions does restrict photosynthetic efficiency.
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在链接到云南高校图书馆文献保障联盟下载...
云南高校图书馆联盟文献共享服务平台 版权所有©
您的IP:216.73.216.222